9CTG: SapNP Reconstituted Human ABCB1

SapNP Reconstituted Human ABCB1 bound to ATP gammaS. Determined by electron microscopy at 3.4 Å resolution. Released 22 Jan 2025.

Method: Electron microscopy
Resolution: 3.4 Å
Organism: Homo sapiens
Chains: 1
Atoms: 9,128
Mol. weight: 147.05 kDa
Ligands: UPL, MG, AGS
Released: 22 Jan 2025

Explore 9CTG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9CTG contains 56 α-helices and 28 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 56 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	38-40	3
α-helix	45-62	18
α-helix	65-68	4
α-helix	69-79	11
α-helix	107-157	51
α-helix	160-165	6
α-helix	169-173	5
α-helix	174-178	5
α-helix	179-185	7
α-helix	189-210	22
α-helix	213-219	7
α-helix	222-259	38
α-helix	261-267	7
α-helix	270-317	48
α-helix	320-323	4
α-helix	328-369	42
β-strand	383	1	1
β-strand	392-399	8	2
β-strand	410-417	8	2
β-strand	422-426	5	3
α-helix	433-440	8
β-strand	448-453	6	2
β-strand	456-457	2	2
β-strand	461	1	1
α-helix	463-468	6
β-strand	470-473	4	3
β-strand	483	1	4
α-helix	484-489	6
α-helix	497-506	10
α-helix	510-515	6
β-strand	523	1	4
α-helix	526-528	3
α-helix	533-546	14
β-strand	551-555	5	3
α-helix	563-575	13
β-strand	581-585	5	3
α-helix	590-593	4
β-strand	597-602	6	3
β-strand	605-608	4	3
α-helix	612-617	6
α-helix	621-629	9
α-helix	698-703	6
α-helix	705-707	3
α-helix	708-722	15
α-helix	727-739	13
α-helix	746-796	51
α-helix	801-804	4
α-helix	811-829	19
α-helix	832-852	21
α-helix	858-862	5
α-helix	865-902	38
α-helix	904-910	7
α-helix	913-923	11
α-helix	925-965	41
α-helix	971-981	11
α-helix	982-984	3
α-helix	985-992	8
α-helix	995-1013	19
β-strand	1026	1	5
β-strand	1035-1042	8	6
β-strand	1053-1060	8	6
β-strand	1065-1069	5	7
α-helix	1077-1083	7
β-strand	1093-1096	4	6
β-strand	1099-1100	2	6
β-strand	1104	1	5
α-helix	1106-1112	7
β-strand	1114-1116	3	7
β-strand	1126	1	8
α-helix	1127-1132	6
α-helix	1142-1151	10
α-helix	1155-1160	6
α-helix	1167	1
β-strand	1168	1	8
α-helix	1169	1
α-helix	1178-1191	14
β-strand	1196-1200	5	7
α-helix	1208-1220	13
β-strand	1226-1230	5	7
α-helix	1234-1238	5
β-strand	1242-1247	6	7
β-strand	1250-1255	6	7
α-helix	1257-1262	6
α-helix	1266-1272	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ATP-dependent translocase ABCB1	A	protein	1280	Homo sapiens	P08183 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9CTG_1 ATP-dependent translocase ABCB1 (chains A)
MDLEGDRNGGAKKKNFFKLNNKSEKDKKEKKPTVSVFSMFRYSNWLDKLYMVVGTLAAII
HGAGLPLMMLVFGEMTDIFANAGNLEDLMSNITNRSDINDTGFFMNLEEDMTRYAYYYSG
IGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVS
KINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFT
DKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIG
AAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARG
AAYEIFKIIDNKPSIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSG
QTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLF
ATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIA
IARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAG
FDDGVIVEKGNHDELMKEKGIYFKLVTMQTAGNEVELENAADESKSEIDALEMSSNDSRS
SLIRKRSTRRSVRGSQAQDRKLSTKEALDESIPPVSFWRIMKLNLTEWPYFVVGVFCAII
NGGLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKA
GEILTKRLRYMVFRSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNI
ANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEA
IENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFG
AYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLIDS
YSTEGLMPNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVV
QLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRVV
SQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLD
EATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQL
LAQKGIYFSMVSVQAGTKRQ

Ligands and cofactors

ID	Name	Formula	Copies
UPL	Unknown branched fragment of phospholipid	C34 H70	9
MG	Magnesium ion	Mg	2
AGS	Phosphothiophosphoric acid-adenylate ester	C10 H16 N5 O12 P3 S	2

Primary citation

Structural insights into binding-site access and ligand recognition by human ABCB1. Kurre, D., Dang, P.X., Le, L.T.M. et al. EMBO J (2025) 44:991-1006. DOI 10.1038/s44318-025-00361-z · PubMed

Other PDB entries of the same protein (UniProt P08183 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8Y6H 2.49 Å, P-glycoprotein in complex with UIC2 Fab and triple elacridar molecules in LMNG detergent
8Y6I 2.54 Å, P-glycoprotein in complex with UIC2 Fab and triple elacridar molecules in nanodisc
7A69 3.2 Å, Nanodisc reconstituted human ABCB1 in complex with MRK16 Fab and vincristine
6C0V 3.4 Å, Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation
7A6F 3.5 Å, Nanodisc reconstituted human ABCB1 in complex with MRK16 Fab and zosuquidar
7O9W 3.5 Å, Encequidar-bound human P-glycoprotein in complex with UIC2-Fab
6FN1 3.58 Å, Zosuquidar and UIC2 Fab complex of human-mouse chimeric ABCB1 (ABCB1HM)
6QEX 3.6 Å, Nanodisc reconstituted human ABCB1 in complex with UIC2 fab and taxol
7A6C 3.6 Å, Nanodisc reconstituted human ABCB1 in complex with MRK16 Fab and elacridar
7A6E 3.6 Å, Nanodisc reconstituted human ABCB1 in complex with MRK16 Fab and tariquidar
9CTC 3.6 Å, SapNP reconstituted Human ABCB1 in complex with Zosuquidar and ATP/Mg
9CR8 3.8 Å, SapNP reconstituted human ABCB1

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